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Microbiology 146 (2000), 2695-2703
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Microbiology (2000), 146, 2695-2703.
© 2000 Society for General Microbiology

Genetics and Molecular Biology

The Aspergillus nidulans cysA gene encodes a novel type of serine O-acetyltransferase which is homologous to homoserine O-acetyltransferases

Marcin Grynberg1, Jacek Topczewskia,1, Adam Godzik2 and Andrzej Paszewski1

Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 5A Pawinskiego St, 02-106 Warszawa, Poland1
The Burnham Institute, 10901 N. Torrey Pines Rd, La Jolla, CA 92037, USA2

Author for correspondence: Andrzej Paszewski. Fax: +48 3912 1623. e-mail: apasz{at}ibb.waw.pl

The Aspergillus nidulans cysA gene was cloned by functional complementation of the cysA1 mutation that impairs the synthesis of O-acetylserine. The molecular nature of cysA1 and cysA103 alleles was characterized; a nucleotide substitution and a frame shift were found in the former and a deletion mutation in the latter. The CYSA protein is 525 amino acids long and is encoded by an uninterrupted open reading frame. Expression of the cysA gene appears not to be regulated by sulfur, carbon and nitrogen sources. Protein sequence analysis reveals extensive similarity to homoserine O-acetyltransferases, particularly the bacterial ones, and no homology with known serine O-acetyltransferases. The authors propose that the CYSA protein is analogous to serine O-acetyltransferases, i.e. it catalyses the same reaction but has an independent evolutionary origin.

Keywords: A. nidulans, cysteine synthesis, analogous genes

Abbreviations: HATase, homoserine O-acetyltransferase; OAS, O-acetylserine; SATase, serine O-acetyltransferase

The GenBank accession number for the sequence reported in this paper is AF029885.

a Present address: Department of Molecular Biology, Vanderbilt University, Box 1820 Station B, Nashville, TN 37235, USA.






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